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Database: UniProt
Entry: D4DF77_TRIVH
LinkDB: D4DF77_TRIVH
Original site: D4DF77_TRIVH 
ID   D4DF77_TRIVH            Unreviewed;      1132 AA.
AC   D4DF77;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Glycerophosphocholine phosphodiesterase Gde1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TRV_05822 {ECO:0000313|EMBL:EFE39504.1};
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE39504.1, ECO:0000313|Proteomes:UP000008383};
RN   [1] {ECO:0000313|Proteomes:UP000008383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFE39504.1}.
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DR   EMBL; ACYE01000335; EFE39504.1; -; Genomic_DNA.
DR   RefSeq; XP_003020128.1; XM_003020082.1.
DR   AlphaFoldDB; D4DF77; -.
DR   GeneID; 9583892; -.
DR   KEGG; tve:TRV_05822; -.
DR   HOGENOM; CLU_005444_1_0_1; -.
DR   OrthoDB; 1005457at2759; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd14484; SPX_GDE1_like; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR030395; GP_PDE_dom.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR004331; SPX_dom.
DR   PANTHER; PTHR22958:SF1; GLYCEROPHOSPHOCHOLINE PHOSPHODIESTERASE GPCPD1; 1.
DR   PANTHER; PTHR22958; GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF03009; GDPD; 1.
DR   Pfam; PF03105; SPX; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS51704; GP_PDE; 1.
DR   PROSITE; PS51382; SPX; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1..141
FT                   /note="SPX"
FT                   /evidence="ECO:0000259|PROSITE:PS51382"
FT   REPEAT          369..401
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          456..488
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          527..559
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          801..1127
FT                   /note="GP-PDE"
FT                   /evidence="ECO:0000259|PROSITE:PS51704"
FT   REGION          587..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          880..913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        883..901
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1132 AA;  124624 MW;  FA4A58446C777BAD CRC64;
     MVPEWSSSYI KYKSLKKLIK SAVQAKKMGN DPDLADYTNT TPGFFYSLDR NLEDVDSFYN
     KKFSDCSRRL KLLEDRFGHP ETLPSHLDPE DTEDLMAALL ELRGQLRKLQ WYGEVNRRGF
     IKITKKLDKK LPGANAQIKY LSTKVNPALF ATNSRLLHSV NSINEWLSVL GHEKVMDDNS
     STHSALSLKK PSSGVILNLP TSLLLSVDDA LRRDDTNALL DLLPTLKTAA DGIGEAVFTK
     VLISLQQRSI FYRSKACLAA LLQRVTSLEE EDDINKRNCI HRLVISIGRS QSTVDPESSA
     TMVLNFPTET SNYITPATTP TLKPQRPVVM ESDHPTHIGR DSPVVMFLQY LLDNLLPHQR
     PALLARDISG KTPLHFAAQY GFKAVCDVII EHLQEWDMFD VSEGIDGPLW QDEDGMAPLH
     LSVVGGHPLT TKTLLDSENW KGSNQDKTAI RRNILKSSAV LALATKANFV DIVHLLVEAG
     VNINYQDEQG ETALHSAARF GHDQCAAALL KGSDEQKANV ELAENTYAWT PLFIASVDGN
     INIVKLLIEA GANLEATDSS GWTAKEHATL RGHIDIARLL DEAMATSDGS VESDTASQSA
     VSSSPPSQCS LNDRNSKDRA PDAVKSFGHR YLTDKSMILV SLGTMDMRKT ADPVSLERIP
     MAEAHLTQLD TALSIVVSAS GAHGEPQIID LPVQDNISTE PIVFHTADSS KTKIVFDLVP
     TYAGSKDEVF GRGVALLSSF KPTVGSSRSN LQGDFVVPLI AAKTLEIIGS VTFNFLVITP
     FSHPKMSITE EQTYWKSVTS PMVIGHRGLG KNIAGRHSLQ LGENTVQVCL NLLQIFDFPN
     SRPSLLSRLQ TWALHMLSET GIDAPVHTLT LEQFLHISDG RKPAGKQSSN HSGTPNSEDG
     FPRLLQTRPR SMSVGEELDV PNLSERMKHT RDFKKKGFKG NSRGDHIQAP FATLEELFKE
     LPKSAGFNME LKYPMLHESE EEEMDTYAVE LNSFVDNVLR IVYDHGEGRN MIFSSFNPDI
     CLLLSFKQPS IPVLFLTDSG VSPVADIRAS SLQEAIRFAS RWNLLGIVTN AEPLVLSPRL
     VKVVKESGLV CVSYGTINND PANVKIQVNE GIDAVIVDSV LAIRQGLTGV EA
//
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